TAILIEUCHUNG - Báo cáo khoa học: Characterization of heme-binding properties of Paracoccus denitrificans Surf1 proteins

Biogenesis of cytochromec oxidase (COX) is a highly complex process involving 30 chaperones in eukaryotes; those required for the incorpora-tion of the copper and heme cofactors are also conserved in bacteria. Surf1, associated with hemeainsertion and with Leigh syndrome if defec-tive in humans, is present as two homologs in the soil bacterium Paracoc-cus denitrificans, Surf1c and Surf1q. | IFEBS Journal Characterization of heme-binding properties of Paracoccus denitrificans Surfl proteins Achim Hannappel1 Freya A. Bundschuh1 and Bernd Ludwig1 2 1 Molecular Genetics Group Institute of Biochemistry Goethe University Frankfurt Frankfurt am Main Germany 2 Cluster of Excellence Macromolecular Complexes Frankfurt am Main Germany Keywords CtaA cytochrome c oxidase heme a synthase Leigh syndrome oxidase assembly Correspondence B. Ludwig Institute of Biochemistry Goethe University Frankfurt Max-von-Laue-Strasse 9 D-60438 Frankfurt am Main Germany Fax 49 69 798 29244 Tel 49 69 798 29237 E-mail ludwig@ Website http . Received 8 February 2011 revised 4 March 2011 accepted 14 March 2011 doi Biogenesis of cytochrome c oxidase COX is a highly complex process involving 30 chaperones in eukaryotes those required for the incorporation of the copper and heme cofactors are also conserved in bacteria. Surf1 associated with heme a insertion and with Leigh syndrome if defective in humans is present as two homologs in the soil bacterium Paracoccus denitrificans Surf1c and Surf1q. In an in vitro interaction assay the heme a transfer from purified heme a synthase CtaA to Surf1c was followed and both Surf proteins were tested for their heme a binding properties. Mutation of four strictly conserved amino acid residues within the transmembrane part of each Surf1 protein confirmed their requirement for heme binding. Interestingly the mutation of a tryptophan residue in transmembrane helix II W200 in Surf1c and W209 in Surf1q led to a drastic switch in the heme composition with Surf1 now being populated mostly by heme o the intermediate in the heme a biosynthetic pathway. This tryptophan residue discriminates between the two heme moieties apparently coordinates the formyl group of heme a and most likely presents the cofactor in a spatial orientation suitable for optimal transfer to its target site .

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